Umena et al., 2006 - Google Patents
The crystal structure of L-lactate oxidase from Aerococcus viridans at 2.1 Å resolution reveals the mechanism of strict substrate recognitionUmena et al., 2006
- Document ID
- 2629635941176703108
- Author
- Umena Y
- Yorita K
- Matsuoka T
- Kita A
- Fukui K
- Morimoto Y
- Publication year
- Publication venue
- Biochemical and biophysical research communications
External Links
Snippet
l-Lactate oxidase (LOX) from Aerococcus viridans is a member of the α-hydroxyacid-oxidase flavoenzyme family. We have determined the three-dimensional structure of LOX and revealed the mechanism of substrate recognition. The LOX monomer structure has a typical …
- 239000000758 substrate 0 title abstract description 23
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- C07—ORGANIC CHEMISTRY
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- C07K2299/00—Coordinates from 3D structures of peptides, e.g. proteins or enzymes
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- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
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- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
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- C12N2500/00—Specific components of cell culture medium
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- C12N2500/32—Amino acids
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- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
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- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
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